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Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH–ubiquinone oxidoreductase (Complex I)
Author(s) -
Albracht Simon P.J.,
Hedderich Reiner
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02172-4
Subject(s) - hydrogenase , oxidoreductase , flavodoxin , ferredoxin , protein subunit , chemistry , nad+ kinase , biochemistry , enzyme , stereochemistry , gene
Hydrogenases have clear evolutionary links to the much more complex NADH–ubiquinone oxidoreductases (Complex I). Certain membrane‐bound [NiFe]‐hydrogenases presumably pump protons. From a detailed comparison of hydrogenases and Complex I, it is concluded here that the TYKY subunit in these enzymes is a special 2[4Fe–4S] ferredoxin, which functions as the electrical driving unit for a proton pump. The comparison further revealed that the flavodoxin fold from [NiFe]‐hydrogenases is presumably conserved in the PSST subunit of Complex I. It is proposed that bovine Complex I and the soluble NAD + ‐reducing hydrogenase from Ralstonia eutropha each contain a second FMN group.